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Information on EC 3.13.1.1 - UDP-sulfoquinovose synthase and Organism(s) Spinacia oleracea and UniProt Accession Q84KI6

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EC Tree
     3 Hydrolases
         3.13 Acting on carbon-sulfur bonds
             3.13.1 Acting on carbon-sulfur bonds
                3.13.1.1 UDP-sulfoquinovose synthase
IUBMB Comments
Requires NAD+, which appears to oxidize UDP-alpha-D-glucose to UDP-4-dehydroglucose, which dehydrates to UDP-4-dehydro-6-deoxygluc-5-enose, to which sulfite is added. The reaction is completed when the substrate is rehydrogenated at C-4. The enzyme from Arabidopsis thaliana is specific for UDP-Glc and sulfite.
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This record set is specific for:
Spinacia oleracea
UNIPROT: Q84KI6
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The taxonomic range for the selected organisms is: Spinacia oleracea
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
udp-sulfoquinovose synthase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
sulfite:UDP-glucose sulfotransferase
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UDPsulfoquinovose synthase
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uridine 5'-diphosphate-sulfoquinovose synthase
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sulfite:UDP-glucose sulfotransferase
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synthase, uridine diphosphosulfoquinovose
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UDP-sulfoquinovose synthase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
UDP-alpha-D-sulfoquinovopyranose + H2O = UDP-alpha-D-glucose + sulfite
show the reaction diagram
required NAD+ appears to oxidize the substrate to UDP-4-dehydroglucose, which dehydrates to UDP-4-dehydro-6-deoxygluc-5-enose, to which sulfite can add, the reaction is completed when the substrate is rehydrogenated at C-4
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of sulfonic acid
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hydrolysis of C-S bond
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SYSTEMATIC NAME
IUBMB Comments
UDP-6-sulfo-6-deoxyglucose sulfohydrolase
Requires NAD+, which appears to oxidize UDP-alpha-D-glucose to UDP-4-dehydroglucose, which dehydrates to UDP-4-dehydro-6-deoxygluc-5-enose, to which sulfite is added. The reaction is completed when the substrate is rehydrogenated at C-4. The enzyme from Arabidopsis thaliana is specific for UDP-Glc and sulfite.
CAS REGISTRY NUMBER
COMMENTARY hide
337378-74-2
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
UDP-glucose + sulfite
UDP-6-sulfoquinovose + H2O
show the reaction diagram
UDP-alpha-D-glucose + sulfite
UDP-alpha-D-sulfoquinovopyranose + H2O
show the reaction diagram
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-
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
UDP-glucose + sulfite
UDP-6-sulfoquinovose + H2O
show the reaction diagram
key enzyme in formation of the sulfolipid head group precursor UDP-sulfoquinovose, sulfoquinovosyldiacylglycerol is a polar lipid present in photosynthetic membranes, enzyme is complexed in vivo with accessory proteins
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?
UDP-alpha-D-glucose + sulfite
UDP-alpha-D-sulfoquinovopyranose + H2O
show the reaction diagram
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-
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-
?
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
additional information
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
Uniprot
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
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SQD1 is a soluble plastid UDP-glucose pyrophosphorylase
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
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UDP-sulfoquinovose synthase, SQD1, is important in sulfoquinovosyldiacylglycerol, SQDG, biosynthesis together with the SQDG synthase, SQD2, mechanism for SQDG biosynthesis, overview. Sulfoquinovosyldiacylglycerol is the only sulfur-containing anionic glycerolipid, a relatively minor relatively minor, and is the least prevalent component of photosynthetic membrane lipids. The function of SQDG under phosphate-limited growth conditions is highly correlated with the regulation of other plant glycerolipid biosyntheses
additional information
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ferredoxin-dependent glutamate synthase, FdGOGAT, co-purifies with the native SQD1 from chloroplast stroma and is tightly associated with the enzyme. FdGOGAT is a flavincontaining protein that can reversibly bind sulfite, suggesting that the protein efficiently delivers sulfite to the SQD1 active site
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
SQD1_SPIOL
482
0
53811
Swiss-Prot
Chloroplast (Reliability: 2)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
250000
46700
x * 46700, calculated from sequence
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 46700, calculated from sequence
dimer
homodimer
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
native enzyme from chloroplasts, recombinant enzyme from Escherichia coli
native enzyme from the chloroplast stroma. Ferredoxin-dependent glutamate synthase, FdGOGAT, co-purifies and is tightly associated with SQD1
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
cDNA isolation and functional expression in Escherichia coli
expression in Escherichia coli
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Shimojima, M.; Benning, C.
Native uridine 5'-diphosphate-sulfoquinovose synthase, SQD1, from spinach purified as a 250-kDa complex
Arch. Biochem. Biophys.
413
123-130
2003
Spinacia oleracea (Q84KI6), Spinacia oleracea
Manually annotated by BRENDA team
Shimojima, M.
Biosynthesis and functions of the plant sulfolipid
Prog. Lipid Res.
50
234-239
2011
Arabidopsis thaliana, Cereibacter sphaeroides, Chlamydomonas reinhardtii, Spinacia oleracea
Manually annotated by BRENDA team